Research workbench
Crystal structure of N-formylglutamate amidohydrolase (YP_297560.1) from ralstonia eutropha JMP134 at 2.00 a resolution
Analyse Crystal structure of N-formylglutamate amidohydrolase (YP_297560.1) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2Q7S
- Type
- protein
- Length
- 551 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- N-formylglutamate amidohydrolase
- UniProt
- Q46VW8
- Ligands
- ZN
- Pockets
- 7 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 37% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N-formylglutamate amidohydrolase | protein | 271 | 37% helix, 18% strand | Q46VW8 |
| B | N-formylglutamate amidohydrolase | protein | 280 | 36% helix, 19% strand | Q46VW8 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 926 | 0.73 | 0.77 | 75 | empty |
| 2 | 339 | 0.60 | 0.77 | 39 | empty |
| 3 | 71 | 0.44 | 0.81 | 25 | empty |
| 4 | 119 | 0.37 | 0.74 | 24 | empty |
| 5 | 64 | 0.32 | 0.75 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 415 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 modified (engineered).
Compared structures
- 2Q7S · Crystal structure of N-formylglutamate amidohydrolase (YP_297560.1) from Ralstonia… · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q46VW8
- Elsewhere: RCSB PDB 2Q7S · PDBe 2Q7S · UniProt Q46VW8
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